ID W5N0F6_LEPOC Unreviewed; 1373 AA.
AC W5N0F6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Vacuolar protein sorting-associated protein 8 homolog {ECO:0000313|Ensembl:ENSLOCP00000014115.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014115.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000014115.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the VPS8 family.
CC {ECO:0000256|ARBA:ARBA00009422}.
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DR EMBL; AHAT01017684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015210004.1; XM_015354518.1.
DR Ensembl; ENSLOCT00000014144.1; ENSLOCP00000014115.1; ENSLOCG00000011461.1.
DR GeneID; 107078254; -.
DR KEGG; loc:107078254; -.
DR GeneTree; ENSGT00390000010672; -.
DR HOGENOM; CLU_000917_1_2_1; -.
DR OrthoDB; 120292at2759; -.
DR Proteomes; UP000018468; Linkage group LG9.
DR Bgee; ENSLOCG00000011461; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR CDD; cd16687; RING-H2_Vps8; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045111; Vps41/Vps8.
DR InterPro; IPR025941; Vps8_central_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR PANTHER; PTHR12616:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 8 HOMOLOG; 1.
DR Pfam; PF12816; Vps8; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 169..210
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1233..1282
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 67..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 153946 MW; 268FE5285598880F CRC64;
MSENEREVVP GSGLFLGISL PEAEELDDKE FNIPVVEIPP TLESILTEDS VIEDNLDPFL
LDEFTLSTEE TGQEDSSTQQ TDESIRRQTS PSPWIKEPPL PDVEQDAVLR CVTLRGVSTQ
IVSAADRVAA GLPTAVAVCG IIAIGTSNGL LLIFDPGQVL KLCLGSTAIG AEKGPISALA
INSNCTHVLC GFANGQILQW DLETGKLLRT IANANPLGNA VVNIKFTDDP SLAVWNDSAG
SVFELHFKRS LGAKAHEVHC LFSSDKGKVY CVEPLNVGEP FTGHSVAQHS LVAMVSLRKV
LIITLKPDLK VVYASPVVKT DAHCIPSLAW NFLWIQESVD PVLAFCQSSC MTMFHVKCTS
ETLSVVKIRE IKLHFEIINF KWMNTQTLLL IDSVEKLHVL DRKSGKELQL LDLPDLQLVH
TCSPSKDWAV GTDATTVNKI TYQSVGSHGG ETILLGVKSV RTVSLRTWAE RLDSLVKQER
HAEALALAWK FSEGSAKAVV GLPGGKQKKK AAVAKKVADI LLDYLELCLR RCPEQGKLQV
MEQHFKEMIP LCATCCFKFN RIDLIFGEVY EKLNHNAVAL GVLFECLEPH ILSSKQNNIP
PLVMKDMVGY YEEQGKVHVL DKLIPHLDIM TLDLHQIVNL SRTFKLCDSL IYVYNKGMND
YTTPIEEMTQ IMSVALRSEK PDDIVSVGNT ILVYISCCLT GREYPLGVVP ETKVQDVKSK
VFMCLTSVHS KDIDPVEDPY PFIRILLKYN TREFLNVLAL TFEDLQQDKQ AVEFHQRIID
ILLQVMLESA DFTPSQIGSL FTFLARQLAK AENSLFVNRR LFHQVLDFLC NPDDTTQHAE
RQQALLELLQ AGGSAYFDES KLLSMAESVQ FYQVCEFVFH EKRLYHRILA CYLKDAARKD
QVLSYIRQIA ARADLTEKEK VLFQNELFCN IQELLELSPD QTSVLILRHY QDSVPIIIET
LQEDSRLLFD FLHGVLNPRA DPWPYKDSSL LNHKVHELYL DLLCQNHPEQ ALLFLKLSDS
YRTEQAAEIV HKYKVYDSLA YLLESQGNTQ AAFSVLFEDL KSSLNNLTQS ATCAETSTES
HSEESGLLST AHTLVQNLIA FCQRASVTLD IKQRKELWFP ILDFTMSPTL HLMSKPPLAF
VRGIKDLTKE VLEAMTSYIP LMDILQKLMQ DTVHTFNNYG EIRTLIFKMF DAYTYEKTLL
ETTRSLLSQD LHSSLCSLKI TVSRGLTPAH KKCAVCSQPY SHGAAGSGVL VFSCGHVYHS
ACLQSSLREQ EGWTEQWACF KCLSPNKRWT SITPGSVNQG SQCFKMDPGQ IEAADCFKRT
FKNPSRISVL MELTRHTSAS LDSFKPEADI FRQSGIFEQP DFKLQLAPPP LIE
//
